1BP5
HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE, APO FORM
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 113 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-11-15 |
| Detector | RIGAKU RAXIS IIC |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 83.500, 77.300, 107.500 |
| Unit cell angles | 90.00, 98.30, 90.00 |
Refinement procedure
| Resolution | 6.000 - 2.200 |
| R-factor | 0.203 |
| Rwork | 0.203 |
| R-free | 0.29200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | INDIVIDUAL DOMAINS OF HUMAN TRANSFERRIN N-TERMINAL HALF-MOLECULE (FE FORM) 1A8E |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.700 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.000 | 2.200 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.046 | 0.271 |
| Number of reflections | 73066 | |
| <I/σ(I)> | 9.2 | 4 |
| Completeness [%] | 79.9 | 61.1 |
| Redundancy | 3.2 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 5.3 | 4 * | PROTEIN WAS CRYSTALLIZED FROM 35% MPD. BUFFER WAS 50MM POTASSIUM ACETATE, PH 5.3, WITH 50MM KCL, AND 20MM NA BICARBONATE CRYSTALS GROWN AT 4 DEGREES C USING THE SITTING DROP METHOD. |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | drop | 20 (mM) | ||
| 3 | 1 | drop | 50 (mM) | ||
| 4 | 1 | reservoir | potassium acetate | 50 (mM) | |
| 5 | 1 | reservoir | MPD | 35 (%(v/v)) |
